ArticlePloS one2014
The negatively charged regions of lactoferrin binding protein B, an adaptation against anti-microbial peptides.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Lactoferrin-Derived Peptides in Cancer Therapy: Structural Features, Mechanistic Insights and Clinical Translation Prospects.International journal of molecular sciences · 2026Review
- Review
- Molecular Mechanisms of Bacterial Resistance to Antimicrobial Peptides in the Modern Era: An Updated Review.Microorganisms · 2024Review
- A secreted bacterial protein protects bacteria from cationic antimicrobial peptides by entrapment in phase-separated droplets.PNAS nexus · 2024Article
- Lactoferrins in Their Interactions with Molecular Targets: A Structure-Based Overview.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Testing Antimicrobial Properties of Human Lactoferrin-Derived Fragments.International journal of molecular sciences · 2023Article
- Structural and functional insights into iron acquisition from lactoferrin and transferrin in Gram-negative bacterial pathogens.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Article
- Targeting bacterial transferrin and lactoferrin receptors for vaccines.Trends in microbiology · 2022Review
- The Host-Pathogen Interactions and Epicellular Lifestyle ofFrontiers in cellular and infection microbiology · 2022Review
- Article
- The Role of theFrontiers in microbiology · 2021Article
- Utility of Hybrid Transferrin Binding Protein Antigens for Protection Against Pathogenic Neisseria Species.Frontiers in immunology · 2019Article
- Innate Nutritional Immunity.Journal of immunology (Baltimore, Md. : 1950) · 2018Review
- Lactoferrin binding protein B - a bi-functional bacterial receptor protein.PLoS pathogens · 2017Article
- Biological Functions of the Secretome ofFrontiers in cellular and infection microbiology · 2017Review
- Antimicrobial Functions of Lactoferrin Promote Genetic Conflicts in Ancient Primates and Modern Humans.PLoS genetics · 2016Article
- Multi-omics analysis on the pathogenicity ofProteome science · 2016Article
- Antimicrobial peptide resistance in Neisseria meningitidis.Biochimica et biophysica acta · 2015Review
- The Iron age of host-microbe interactions.EMBO reports · 2015Review
- The structure of lactoferrin-binding protein B from Neisseria meningitidis suggests roles in iron acquisition and neutralization of host defences.Acta crystallographica. Section F, Structural biology communications · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactoferrin binding protein B (LbpB) is a bi-lobed membrane bound lipoprotein that is part of the lactoferrin receptor complex in a variety of Gram-negative pathogens. Despite high sequence diversity among LbpBs from various strains and species, a cluster of negatively charged amino acids is invariably present in the protein's C-terminal lobe in all species except Moraxella bovis. The function of LbpB in iron acquisition has yet to be experimentally demonstrated, whereas in vitro studies have shown that LbpB confers protection against lactoferricin, a short cationic antimicrobial peptide released from the N- terminus of lactoferrin. In this study we demonstrate that the negatively charged regions can be removed from the Neisseria meningitidis LbpB without compromising stability, and this results in the inability of LbpB to protect against the bactericidal effects of lactoferricin. The release of LbpB from the cell surface by the autotransporter NalP reduces the protection against lactoferricin in the in vitro killing assay, attributed to removal of LbpB during washing steps, but is unlikely to have a similar impact in vivo. The protective effect of the negatively charged polysaccharide capsule in the killing assay was less than the protection conferred by LbpB, suggesting that LbpB plays a major role in protection against cationic antimicrobial peptides in vivo. The selective release of LbpB by NalP has been proposed to be a mechanism for evading the adaptive immune response, by reducing the antibody binding to the cell surface, but may also provide insights into the primary function of LbpB in vivo. Although TbpB and LbpB have been shown to be major targets of the human immune response, the selective release of LbpB suggests that unlike TbpB, LbpB may not be essential for iron acquisition, but important for protection against cationic antimicrobial peptides.
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